Structure of PDB 1y6f Chain A Binding Site BS02
Receptor Information
>1y6f Chain A (length=394) Species:
10665
(Tequatrovirus T4) [
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MGSMRICIFMARGLEGCGVTKFSLEQRDWFIKNGHEVTLVYAKDKSFTRT
SSHDHKSFSIPVILAKEYDKALKLVNDCDILIINSVPATSVQEATINNYK
KLLDNIKPSIRVVVYQHDHSVLSLRRNLGLEETVRRADVIFSHSDNGDFN
KVLMKEWYPEEAPTVYNFQPPMDIVKVRSTYWKDVSEINMNINRWIGRTT
TWKGFYQMFDFHEKFLKPAGKSTVMEGLERSPAFIAIKEKGIPYEYYGNR
EIDKMNLAPNQPAQILDCYINSEMLERMSKSGFGYQLSKLNQKYLQRSLE
YTHLELGACGTIPVFWKSTGENLKFRVDNTPLTSHDSGIIWFDENDMEST
FERIKELSSDRALYDREREKAYEFLYQHQDSSFCFKEQFDIITK
Ligand information
>1y6f Chain D (length=13) [
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ctatctgagtatc
Receptor-Ligand Complex Structure
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PDB
1y6f
Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase.
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
R1122 R1236 S1237 P1238 I1241 R1256
Binding residue
(residue number reindexed from 1)
R125 R230 S231 P232 I235 R250
Enzymatic activity
Enzyme Commision number
2.4.1.26
: DNA alpha-glucosyltransferase.
Gene Ontology
Molecular Function
GO:0016757
glycosyltransferase activity
GO:0033820
DNA alpha-glucosyltransferase activity
Biological Process
GO:0006304
DNA modification
GO:0019049
virus-mediated perturbation of host defense response
GO:0039504
symbiont-mediated suppression of host adaptive immune response
GO:0098672
symbiont-mediated suppression of host CRISPR-cas system
GO:0099018
symbiont-mediated evasion of host restriction-modification system
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Molecular Function
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Biological Process
External links
PDB
RCSB:1y6f
,
PDBe:1y6f
,
PDBj:1y6f
PDBsum
1y6f
PubMed
16081100
UniProt
P04519
|GSTA_BPT4 DNA alpha-glucosyltransferase (Gene Name=agt)
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